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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2002-3-22
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pubmed:abstractText |
Mammalian aquaporins are part of the diverse major intrinsic protein family of water and solute channels. Intriguing links exist in structural and functional properties between aquaporins and ion channels. A novel role for aquaporin-1 as a gated ion channel reshapes our current views of this ancient family of transmembrane channel proteins.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0886-1714
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
68-72
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
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pubmed:year |
2002
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pubmed:articleTitle |
New roles for old holes: ion channel function in aquaporin-1.
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pubmed:affiliation |
Department of Physiology, University of Arizona College of Medicine, Tucson, Arizona 85724-5051, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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